1.

The role of initial oligomers in amyloid fibril formation by human stefin B

In this work our group managed to improve the model for teh mechanism of amyloid fibril formation by stefin B - as an appropriate model. We included in the simulation the transformation of initial oligomers.

COBISS.SI-ID: 26998567

2.

Membrane damage by an [alpha]-helical pore forming protein Equinatoxin II proceeds through succesion of ordered steps

As amyloid forming proteins resemble pore forming toxins, this study bears relevance to this project. PI contributed with conformational and kinetical studies of these steps.

COBISS.SI-ID: 2836815

3.

Influence of partial unfolding and aggregation of human stefin B (cystatin B) EPM1 mutants G50E and Q71P on selective cleavages by cathepsins B and S

In this paper Mira P- et al., have determined how EPM1 mutants cleavages occur. This is important as a more open structure of the mutants allows cathepsins to process them faster and thus to lose any inhibitory activity and even worse, to promote aggregation.

COBISS.SI-ID: 26511655